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Manganese in PDB 5lih: Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain

Enzymatic activity of Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain

All present enzymatic activity of Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain:
2.7.11.13;

Protein crystallography data

The structure of Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain, PDB code: 5lih was solved by E.V.Soriano, A.G.Purkiss, N.Q.Mcdonald, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 67.28 / 3.25
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 78.980, 84.230, 111.830, 90.00, 90.00, 90.00
R / Rfree (%) 25.7 / 28.4

Other elements in 5lih:

The structure of Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain also contains other interesting chemical elements:

Fluorine (F) 12 atoms
Aluminium (Al) 4 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain (pdb code 5lih). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 5 binding sites of Manganese where determined in the Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain, PDB code: 5lih:
Jump to Manganese binding site number: 1; 2; 3; 4; 5;

Manganese binding site 1 out of 5 in 5lih

Go back to Manganese Binding Sites List in 5lih
Manganese binding site 1 out of 5 in the Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn603

b:31.8
occ:1.00
 O1A A:ADP601 1.8 33.5 1.0
F1 A:AF3605 2.0 22.1 1.0
OD1 A:ASN383 2.4 31.2 0.5
OD1 A:ASN383 2.4 31.2 0.5
O1B A:ADP601 3.0 40.8 1.0
OD2 A:ASP396 3.0 34.3 1.0
PA A:ADP601 3.2 33.9 1.0
CG A:ASN383 3.6 30.5 0.5
CG A:ASN383 3.6 30.5 0.5
AL A:AF3605 3.6 54.5 1.0
C5' A:ADP601 3.6 36.2 1.0
CG A:ASP396 3.8 34.4 1.0
O5' A:ADP601 3.8 31.4 1.0
CB A:ASP396 3.9 34.8 1.0
C3' A:ADP601 4.0 30.0 1.0
CB A:ASP382 4.0 36.9 1.0
O3A A:ADP601 4.1 36.4 1.0
PB A:ADP601 4.1 45.0 1.0
CE A:LYS380 4.1 31.4 1.0
O3' A:ADP601 4.2 28.8 1.0
ND2 A:ASN383 4.3 29.8 0.5
ND2 A:ASN383 4.3 29.8 0.5
O2A A:ADP601 4.3 34.3 1.0
O A:ASP382 4.3 35.0 1.0
C A:ASP382 4.3 34.8 1.0
C4' A:ADP601 4.4 31.3 1.0
N A:ASN383 4.5 31.9 1.0
O2B A:ADP601 4.5 43.8 1.0
CA A:ASN383 4.6 31.6 0.5
CA A:ASN383 4.6 31.6 0.5
F2 A:AF3605 4.6 63.9 1.0
F3 A:AF3605 4.6 34.8 1.0
CB A:ASN383 4.7 30.7 0.5
CB A:ASN383 4.7 30.7 0.5
CA A:ASP382 4.8 36.0 1.0
OD1 A:ASP396 4.9 34.5 1.0

Manganese binding site 2 out of 5 in 5lih

Go back to Manganese Binding Sites List in 5lih
Manganese binding site 2 out of 5 in the Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn604

b:38.7
occ:1.00
 OD1 A:ASP396 1.9 34.5 1.0
F3 A:AF3605 2.0 34.8 1.0
O2B A:ADP601 2.3 43.8 1.0
CG A:ASP396 2.6 34.4 1.0
OD2 A:ASP396 2.7 34.3 1.0
AL A:AF3605 3.6 54.5 1.0
PB A:ADP601 3.7 45.0 1.0
NZ A:LYS283 3.7 34.2 1.0
CA A:GLY398 4.0 36.5 1.0
O A:HOH708 4.0 25.6 1.0
N A:GLY398 4.0 36.5 1.0
CB A:ASP396 4.1 34.8 1.0
OG F:SER11 4.1 43.9 1.0
O1B A:ADP601 4.1 40.8 1.0
OD2 A:ASP378 4.2 30.9 1.0
F1 A:AF3605 4.3 22.1 1.0
CD2 A:TYR265 4.5 36.2 1.0
O3A A:ADP601 4.5 36.4 1.0
O3B A:ADP601 4.6 58.6 1.0
CE A:LYS283 4.7 34.2 1.0
C A:ASP396 4.7 35.3 1.0
CA A:ASP396 4.7 35.4 1.0
O A:ASP396 4.8 34.4 1.0
O1A A:ADP601 4.8 33.5 1.0
CB A:TYR265 4.9 36.0 1.0
C A:GLY398 4.9 36.5 1.0
F2 A:AF3605 5.0 63.9 1.0

Manganese binding site 3 out of 5 in 5lih

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Manganese binding site 3 out of 5 in the Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn607

b:56.4
occ:1.00
 NE2 A:HIS354 2.8 41.1 1.0
CE1 A:HIS354 3.5 40.7 1.0
CD2 A:HIS354 3.9 39.3 1.0
O A:PRO538 4.6 43.2 1.0
ND1 A:HIS354 4.7 38.7 1.0
CB A:PRO538 4.9 40.2 1.0
CG A:HIS354 4.9 37.8 1.0

Manganese binding site 4 out of 5 in 5lih

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Manganese binding site 4 out of 5 in the Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn603

b:50.6
occ:1.00
 F1 B:AF3605 1.9 26.9 1.0
O1A B:ADP601 1.9 46.0 1.0
OD1 B:ASN383 2.3 37.9 1.0
OD2 B:ASP396 2.6 41.9 1.0
O1B B:ADP601 2.8 44.1 1.0
PA B:ADP601 3.4 49.1 1.0
CG B:ASN383 3.4 37.1 1.0
CG B:ASP396 3.5 41.8 1.0
AL B:AF3605 3.6 59.4 1.0
CE B:LYS380 3.7 39.0 1.0
CB B:ASP396 3.8 41.6 1.0
PB B:ADP601 4.0 38.5 1.0
ND2 B:ASN383 4.0 36.5 1.0
MN B:MN604 4.1 40.7 1.0
CB B:ASP382 4.1 42.5 1.0
O3A B:ADP601 4.1 45.9 1.0
O B:ASP382 4.2 43.8 1.0
C5' B:ADP601 4.2 44.2 1.0
O2A B:ADP601 4.3 48.6 1.0
O5' B:ADP601 4.3 49.0 1.0
C B:ASP382 4.4 42.8 1.0
O3B B:ADP601 4.5 46.1 1.0
F2 B:AF3605 4.6 68.7 1.0
CB B:ASN383 4.6 37.1 1.0
N B:ASN383 4.6 37.5 1.0
OD1 B:ASP396 4.6 42.6 1.0
C3' B:ADP601 4.7 46.5 1.0
CA B:ASN383 4.7 37.9 1.0
F3 B:AF3605 4.8 39.6 1.0
O3' B:ADP601 4.9 46.9 1.0
CA B:ASP382 4.9 42.6 1.0

Manganese binding site 5 out of 5 in 5lih

Go back to Manganese Binding Sites List in 5lih
Manganese binding site 5 out of 5 in the Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 5 of Structure of A Peptide-Substrate Bound to Pkciota Core Kinase Domain within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn604

b:40.7
occ:1.00
 OD2 B:ASP396 2.1 41.9 1.0
F3 B:AF3605 2.1 39.6 1.0
OD1 B:ASP396 2.3 42.6 1.0
O3B B:ADP601 2.3 46.1 1.0
CG B:ASP396 2.5 41.8 1.0
O B:HOH705 2.5 37.6 1.0
AL B:AF3605 2.9 59.4 1.0
O1B B:ADP601 2.9 44.1 1.0
F1 B:AF3605 2.9 26.9 1.0
PB B:ADP601 3.1 38.5 1.0
OD2 B:ASP378 3.9 41.2 1.0
OG G:SER11 4.0 48.4 1.0
CB B:ASP396 4.0 41.6 1.0
MN B:MN603 4.1 50.6 1.0
O2B B:ADP601 4.1 38.3 1.0
O3A B:ADP601 4.3 45.9 1.0
NZ B:LYS283 4.4 43.7 1.0
O1A B:ADP601 4.4 46.0 1.0
CD2 B:TYR265 4.6 45.4 1.0
F2 B:AF3605 4.6 68.7 1.0
CB G:SER11 4.6 46.9 1.0
PA B:ADP601 4.8 49.1 1.0
CA B:ASP396 4.9 42.7 1.0
N B:GLY398 4.9 44.4 1.0
CA B:GLY398 4.9 45.3 1.0

Reference:

E.V.Soriano, M.E.Ivanova, G.Fletcher, P.Riou, P.P.Knowles, K.Barnouin, A.Purkiss, B.Kostelecky, P.Saiu, M.Linch, A.Elbediwy, S.Kjr, N.O'reilly, A.P.Snijders, P.J.Parker, B.J.Thompson, N.Q.Mcdonald. Apkc Inhibition By PAR3 CR3 Flanking Regions Controls Substrate Access and Underpins Apical-Junctional Polarization. Dev.Cell V. 38 384 2016.
ISSN: ISSN 1534-5807
PubMed: 27554858
DOI: 10.1016/J.DEVCEL.2016.07.018
Page generated: Tue Dec 15 04:43:38 2020

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